MAP1C_ARATH
ID MAP1C_ARATH Reviewed; 344 AA.
AC Q9FV51; Q9LS05;
DT 24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 2.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Methionine aminopeptidase 1C, chloroplastic/mitochondrial {ECO:0000255|HAMAP-Rule:MF_03174};
DE Short=MAP 1C {ECO:0000255|HAMAP-Rule:MF_03174};
DE Short=MetAP 1C {ECO:0000255|HAMAP-Rule:MF_03174};
DE EC=3.4.11.18 {ECO:0000255|HAMAP-Rule:MF_03174};
DE AltName: Full=Peptidase M 1C {ECO:0000255|HAMAP-Rule:MF_03174};
DE Flags: Precursor;
GN Name=MAP1C; OrderedLocusNames=At3g25740; ORFNames=K13N2.8;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=11060042; DOI=10.1093/emboj/19.21.5916;
RA Giglione C., Serero A., Pierre M., Boisson B., Meinnel T.;
RT "Identification of eukaryotic peptide deformylases reveals universality of
RT N-terminal protein processing mechanisms.";
RL EMBO J. 19:5916-5929(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10819329; DOI=10.1093/dnares/7.2.131;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:131-135(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
CC -!- FUNCTION: Removes the N-terminal methionine from nascent proteins. The
CC N-terminal methionine is often cleaved when the second residue in the
CC primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser,
CC Thr, or Val). {ECO:0000255|HAMAP-Rule:MF_03174}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Release of N-terminal amino acids, preferentially methionine,
CC from peptides and arylamides.; EC=3.4.11.18;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03174};
CC -!- COFACTOR:
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03174};
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03174};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03174};
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03174};
CC Note=Binds 2 divalent metal cations per subunit. Has a high-affinity
CC and a low affinity metal-binding site. The true nature of the
CC physiological cofactor is under debate. The enzyme is active with
CC cobalt, zinc, manganese or divalent iron ions. Most likely, methionine
CC aminopeptidases function as mononuclear Fe(2+)-metalloproteases under
CC physiological conditions, and the catalytically relevant metal-binding
CC site has been assigned to the histidine-containing high-affinity site.
CC {ECO:0000255|HAMAP-Rule:MF_03174};
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255|HAMAP-
CC Rule:MF_03174, ECO:0000269|PubMed:11060042}. Mitochondrion
CC {ECO:0000255|HAMAP-Rule:MF_03174, ECO:0000269|PubMed:11060042}.
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:11060042}.
CC -!- SIMILARITY: Belongs to the peptidase M24A family. Methionine
CC aminopeptidase type 1 subfamily. {ECO:0000255|HAMAP-Rule:MF_03174}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA95761.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF250962; AAG33976.1; -; mRNA.
DR EMBL; AB028607; BAA95761.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE77063.1; -; Genomic_DNA.
DR RefSeq; NP_189202.1; NM_113473.3.
DR AlphaFoldDB; Q9FV51; -.
DR SMR; Q9FV51; -.
DR STRING; 3702.AT3G25740.1; -.
DR MEROPS; M24.A07; -.
DR PaxDb; Q9FV51; -.
DR PRIDE; Q9FV51; -.
DR ProteomicsDB; 238844; -.
DR EnsemblPlants; AT3G25740.1; AT3G25740.1; AT3G25740.
DR GeneID; 822165; -.
DR Gramene; AT3G25740.1; AT3G25740.1; AT3G25740.
DR KEGG; ath:AT3G25740; -.
DR Araport; AT3G25740; -.
DR TAIR; locus:2085979; AT3G25740.
DR eggNOG; KOG2738; Eukaryota.
DR HOGENOM; CLU_015857_1_5_1; -.
DR InParanoid; Q9FV51; -.
DR OMA; YELEYMI; -.
DR OrthoDB; 1002357at2759; -.
DR PhylomeDB; Q9FV51; -.
DR PRO; PR:Q9FV51; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9FV51; baseline and differential.
DR Genevisible; Q9FV51; AT.
DR GO; GO:0009507; C:chloroplast; TAS:TAIR.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0070006; F:metalloaminopeptidase activity; IBA:GO_Central.
DR GO; GO:0031365; P:N-terminal protein amino acid modification; TAS:TAIR.
DR GO; GO:0070084; P:protein initiator methionine removal; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd01086; MetAP1; 1.
DR Gene3D; 3.90.230.10; -; 1.
DR HAMAP; MF_01974; MetAP_1; 1.
DR InterPro; IPR036005; Creatinase/aminopeptidase-like.
DR InterPro; IPR000994; Pept_M24.
DR InterPro; IPR001714; Pept_M24_MAP.
DR InterPro; IPR002467; Pept_M24A_MAP1.
DR Pfam; PF00557; Peptidase_M24; 1.
DR PRINTS; PR00599; MAPEPTIDASE.
DR SUPFAM; SSF55920; SSF55920; 1.
DR TIGRFAMs; TIGR00500; met_pdase_I; 1.
PE 2: Evidence at transcript level;
KW Aminopeptidase; Chloroplast; Hydrolase; Metal-binding; Mitochondrion;
KW Plastid; Protease; Reference proteome; Transit peptide.
FT TRANSIT 1..?
FT /note="Chloroplast and mitochondrion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03174"
FT CHAIN ?..344
FT /note="Methionine aminopeptidase 1C,
FT chloroplastic/mitochondrial"
FT /id="PRO_0000045806"
FT BINDING 172
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03174"
FT BINDING 189
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03174"
FT BINDING 200
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03174"
FT BINDING 200
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03174"
FT BINDING 262
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03174"
FT BINDING 269
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03174"
FT BINDING 296
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03174"
FT BINDING 327
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03174"
FT BINDING 327
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03174"
FT CONFLICT 264
FT /note="V -> L (in Ref. 1; AAG33976)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 344 AA; 37679 MW; ABD84A7FF64D70BA CRC64;
MLQKISQSIS LCNGDQFKPL IYLAGAPTNF ISSPLSGKKK SSSLRIKRIQ QLQSTLEDRI
NPPLVCGTVS PRLSVPDHIL KPLYVESSKV PEISSELQIP DSIGIVKMKK ACELAARVLD
YAGTLVRPFV TTDEIDKAVH QMVIEFGAYP SPLGYGGFPK SVCTSVNECM FHGIPDSRPL
QNGDIINIDV AVYLDGYHGD TSKTFLCGDV NGSLKQLVKV TEECLEKGIS VCKDGASFKQ
IGKIISEHAA KYGYNMERFI GHGVGTVLHS EPLIYLHSNY DYELEYMIEG QTFTLEPILT
IGTTEFVTWP DKWTIVTADG GPAAQFEHTI LITTTGAEIL TISS
